eF-site ID 4uir-B
PDB Code 4uir
Chain B

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Title Structure of oleate hydratase from Elizabethkingia meningoseptica
Classification LYASE
Compound OLEATE HYDRATASE
Source Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) (OLHYD_ELIME)
Sequence B:  NPITSKFDKVLNASSEYGHVNHEPDSSKEQQRNTPQKSMP
FSDQIGNYQRNKGIPVQSYDNSKIYIIGSGIAGMSAAYYF
IRDGHVPAKNITFLEQLHIDGGSLDGAGNPTDGYIIREMD
MTYENLWDMFQDIPALEMPAPYSVLDEYRLINDNDSNYSK
ARLINNKGEIKDFSKFGLNKMDQLAIIRLLLKNKEELDDL
TIEDYFSESFLKSNFWTFWRTMFAFENWHSLLELKLYMHR
FLHAIDGLNDLSSLVFPKYNQYDTFVTPLRKFLQEKGVNI
HLNTLVKDLDIHINTEGKVVEGIITEQDGKEVKIPVGKND
YVIVTTGSMTEDTFYGNNKTAPIIGIDNSTSGQSAGWKLW
KNLAAKSEIFGKPEKFCSNIEKSAWESATLTCKPSALIDK
LKEYSVNDPYSGKTVTGGIITITDSNWLMSFTCNRQPHFP
EQPDDVLVLWVYALFMDKEGNYIKKTMLECTGDEILAELC
YHLGIEDQLENVQKNTIVRTAFMPYITSMFMPRAKGDRPR
VVPEGCKNLGLVGQFVETNNDVVFTMESSVRTARIAVYKL
LNLNKQVPDINPLQYDIRHLLKAAKTLNDDKPFVGEGLLR
KVLKGTYFEHVLPAGAAEEESFIAEHVNKFREWV
Description


Functional site

1) chain B
residue 599
type
sequence G
description BINDING SITE FOR RESIDUE PO4 B 1642
source : AC2

2) chain B
residue 600
type
sequence E
description BINDING SITE FOR RESIDUE PO4 B 1642
source : AC2

3) chain B
residue 601
type
sequence G
description BINDING SITE FOR RESIDUE PO4 B 1642
source : AC2

4) chain B
residue 602
type
sequence L
description BINDING SITE FOR RESIDUE PO4 B 1642
source : AC2

5) chain B
residue 250
type
sequence D
description BINDING SITE FOR RESIDUE NA B 1643
source : AC4

6) chain B
residue 253
type
sequence N
description BINDING SITE FOR RESIDUE NA B 1643
source : AC4

7) chain B
residue 122
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:26077980
source Swiss-Prot : SWS_FT_FI1

8) chain B
residue 241
type ACT_SITE
sequence Y
description Proton donor => ECO:0000305|PubMed:26077980
source Swiss-Prot : SWS_FT_FI2

9) chain B
residue 73
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR
source Swiss-Prot : SWS_FT_FI3

10) chain B
residue 96
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR
source Swiss-Prot : SWS_FT_FI3

11) chain B
residue 97
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR
source Swiss-Prot : SWS_FT_FI3

12) chain B
residue 104
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR
source Swiss-Prot : SWS_FT_FI3

13) chain B
residue 122
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR
source Swiss-Prot : SWS_FT_FI3

14) chain B
residue 127
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR
source Swiss-Prot : SWS_FT_FI3

15) chain B
residue 290
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR
source Swiss-Prot : SWS_FT_FI3

16) chain B
residue 332
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR
source Swiss-Prot : SWS_FT_FI3

17) chain B
residue 549
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR
source Swiss-Prot : SWS_FT_FI3

18) chain B
residue 553
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR
source Swiss-Prot : SWS_FT_FI3


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